Evidence map›Paper›PMID 25793944›Full record

ArticleNucleus (Austin, Tex.)2015

Phosphorylation of lamins determine their structural properties and signaling functions.

Elin Torvaldson, Vitaly Kochin, John E Eriksson

Abstract read
In one paragraph

Article in Nucleus (Austin, Tex.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

59 citing papers in PubMed.

  1. Review
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  7. Cells · 2025
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Elin Torvaldsona Department of Biosciences; Åbo Akademi University ; Turku , Finland.
Vitaly Kochin
John E Eriksson

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lamin A/C is part of the nuclear lamina, a meshwork of intermediate filaments underlying the inner nuclear membrane. The lamin network is anchoring a complex set of structural and linker proteins and is either directly or through partner proteins also associated or interacting with a number of signaling protein and transcription factors. During mitosis the nuclear lamina is dissociated by well established phosphorylation- dependent mechanisms. A-type lamins are, however, also phosphorylated during interphase. A recent study identified 20 interphase phosphorylation sites on lamin A/C and explored their functions related to lamin dynamics; movements, localization and solubility. Here we discuss these findings in the light of lamin functions in health and disease.

Indexed as

MitosisSignal TransductionAnimalsCaenorhabditis elegansGene Expression RegulationHeLa CellsHumansIntermediate FilamentsInterphaseLamin Type AMuscular Dystrophy, Emery-DreifussMutationNuclear LaminaPhosphorylationProtein TransportSolubilityLamin Type ALMNA protein, humanEDMD, Emery-Dreifuss muscular dystrophyGFP, green fluorescent proteinIFs, intermediate filamentsintermediate filamentslamin A/ClaminopathylaminsLAP2α, Lamina-associated polypeptide 2 isoform αphosphorylationsignaling

Identifiers

PMID25793944
PMCPMC4615644

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.